1.B.32.1.1
Non-specific FomA porin precursor (Kleivdal et al. 1995). The N-terminal region is periplasmic while the C-terminus is a 14 stranded β-barrel (Puntervoll et al. 2002). The β-barrel may have a tilt angle of 45° relative to the barrel axis (Anbazhagan et al., 2008). FomA is fusogenic (Pszon-Bartosz et al., 2011). Its unique solute transport activity with size exclusion limit has been described (Kattner et al. 2015). FomA is a voltage-dependent porin, predicted to form a 14 stranded beta-barrel. It folds in a range of model membranes of very different phospholipid compositions. A study on FomA folding into lipid bilayers indicated the presence of parallel folding pathways for OMPs with larger transmembrane beta-barrels (Kleinschmidt 2006).
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| Accession Number: | Q47905 |
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| Protein Name: | FomA |
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| Length: | 370 |
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| Molecular Weight: | 42241.00 |
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| Species: | Fusobacterium nucleatum subsp [76857] |
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| Number of TMSs: | 1 |
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| Location1 / Topology2 / Orientation3: |
Cell outer membrane1 / Multi-pass membrane protein2 |
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| Substrate |
molecule |
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[1] “Sequence variability of the 40-kDa outer membrane proteins of Fusobacterium nucleatum strains and a model for the topology of the proteins.” Bolstad A.I. et.al. 8041356
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1: MKKLALVLGL LLVVGSVASA KEVMPAPTPA PEKVVEYVEK PVIVYRDREV APAWRPNGSV
61: DVQYRWYGEV EKKNPKDDKD ENWATGKVNA GRLQTLTKVN FTEKQTLEVR TRNHHTLNDT
121: DANNKKSNGA ADEYRLRHFY NFGKLGSSKV NATSRVEFKQ KTNDGEKSLG ASVLFDFADY
181: IYSNNFFKVD KLGLRPGYKY VWKGHGNGEE GTPTVHNEYH LAFESDFTLP FNFALNLEYD
241: LSYNRYREKF ETTDGLKKAE WYGELTAVLS NYTPLYKAGA FELGFNAEGG YDTYNMHQYK
301: RIGGEDGTSV DRRDYELYLE PTLQVSYKPT DFVKLYAAAG ADYRNRITGE SEVKRWRWQP
361: TASAGMKVTF